Sandbox Reserved 773: Difference between revisions
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The numerous hydrogen bond interaction between the enzyme and PLP restrict the translation of the substrate or cofactor. In addition, the negative charges of phosphate group of PLP is stabilized by dipole moment from the neighboring N-terminus of the helix α5 seen in Figure 4 <ref name=jbc/>. These hydrogen bonding and | The numerous hydrogen bond interaction between the enzyme and PLP restrict the translation of the substrate or cofactor. In addition, the negative charges of phosphate group of PLP is stabilized by dipole moment from the neighboring N-terminus of the helix α5 seen in Figure 4 <ref name=jbc/>. These hydrogen bonding and dipole moments create a stable environment for PLP to stay in place during the transitional state through proximity effect. | ||
Additionally, the side chains of Thr-248 and Asp-273 are thought to be responsible for the protonation of the Oxide group and Nitrogen atom in the pyridine ring of PLP during the catalytic mechanism <ref name=jbc/>. | Additionally, the side chains of Thr-248 and Asp-273 are thought to be responsible for the protonation of the Oxide group and Nitrogen atom in the pyridine ring of PLP during the catalytic mechanism <ref name=jbc/>. | ||
== Pathways and Implications== | == Pathways and Implications== | ||
